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Database: PDB
Entry: 4HPU
LinkDB: 4HPU
Original site: 4HPU 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       24-OCT-12   4HPU              
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN  
TITLE    2 KINASE DISPLAYING PARTIAL PHOSPHORYL TRANSFER OF AMP-PNP ONTO A      
TITLE    3 SUBSTRATE PEPTIDE                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: E;                                                            
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;             
COMPND   9 CHAIN: I;                                                            
COMPND  10 FRAGMENT: SP20 PEPTIDE DERIVED FROM CAMP-DEPENDENT PROTEIN KINASE    
COMPND  11 INHIBITOR ALPHA (UNP RESIDUES 6-25);                                 
COMPND  12 SYNONYM: PKI-ALPHA, CAMP-DEPENDENT PROTEIN KINASE INHIBITOR,         
COMPND  13 MUSCLE/BRAIN ISOFORM;                                                
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 OTHER_DETAILS: SYNTHETIC PEPTIDE                                     
KEYWDS    PROTEIN KINASE FOLD, PHOSPHOTRANSFERASE, REGULATORY SUBUNITS, PKI,    
KEYWDS   2 MAGNESIUM, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE INHIBITOR        
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.BASTIDAS,J.M.STEICHEN,J.WU,S.S.TAYLOR                             
REVDAT   5   15-NOV-17 4HPU    1       REMARK                                   
REVDAT   4   10-APR-13 4HPU    1       JRNL                                     
REVDAT   3   03-APR-13 4HPU    1       REMARK                                   
REVDAT   2   27-MAR-13 4HPU    1       JRNL                                     
REVDAT   1   20-MAR-13 4HPU    0                                                
JRNL        AUTH   A.C.BASTIDAS,M.S.DEAL,J.M.STEICHEN,Y.GUO,J.WU,S.S.TAYLOR     
JRNL        TITL   PHOSPHORYL TRANSFER BY PROTEIN KINASE A IS CAPTURED IN A     
JRNL        TITL 2 CRYSTAL LATTICE.                                             
JRNL        REF    J.AM.CHEM.SOC.                V. 135  4788 2013              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   23458248                                                     
JRNL        DOI    10.1021/JA312237Q                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 61.91                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 62785                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.194                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3357                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4566                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 248                          
REMARK   3   BIN FREE R VALUE                    : 0.2580                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2936                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 432                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.57000                                              
REMARK   3    B22 (A**2) : -0.53000                                             
REMARK   3    B33 (A**2) : -0.03000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.072         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.072         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.042         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.523         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3138 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4266 ; 1.329 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   378 ; 5.394 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   151 ;35.373 ;23.974       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   552 ;13.293 ;15.082       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;17.404 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   450 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2349 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1815 ; 0.666 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2937 ; 1.253 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1323 ; 1.860 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1319 ; 3.011 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    12        E   350                          
REMARK   3    RESIDUE RANGE :   E   402        E   402                          
REMARK   3    RESIDUE RANGE :   I   600        I   600                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.0944  13.3922 -20.9222              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0112 T22:   0.0083                                     
REMARK   3      T33:   0.0164 T12:  -0.0022                                     
REMARK   3      T13:  -0.0002 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0608 L22:   0.2169                                     
REMARK   3      L33:   0.4220 L12:  -0.0185                                     
REMARK   3      L13:  -0.0482 L23:   0.1696                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0140 S12:  -0.0095 S13:  -0.0136                       
REMARK   3      S21:  -0.0270 S22:   0.0002 S23:   0.0304                       
REMARK   3      S31:  -0.0139 S32:   0.0076 S33:   0.0138                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     5        I    23                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8220   1.3754 -26.3031              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0214 T22:   0.0170                                     
REMARK   3      T33:   0.0176 T12:   0.0129                                     
REMARK   3      T13:   0.0008 T23:  -0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3179 L22:   1.9079                                     
REMARK   3      L33:   1.4195 L12:  -0.7723                                     
REMARK   3      L13:  -0.5888 L23:   1.2815                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0156 S12:  -0.0234 S13:   0.0277                       
REMARK   3      S21:   0.0139 S22:   0.0328 S23:  -0.0912                       
REMARK   3      S31:   0.0516 S32:   0.0328 S33:  -0.0173                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   501        E   882                          
REMARK   3    RESIDUE RANGE :   I   701        I   750                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.5788  12.4899 -19.0227              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0037 T22:   0.0103                                     
REMARK   3      T33:   0.0115 T12:   0.0016                                     
REMARK   3      T13:   0.0016 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0935 L22:   0.2012                                     
REMARK   3      L33:   0.5454 L12:  -0.0085                                     
REMARK   3      L13:  -0.0403 L23:   0.1815                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0079 S12:  -0.0140 S13:  -0.0111                       
REMARK   3      S21:  -0.0237 S22:  -0.0103 S23:   0.0178                       
REMARK   3      S31:  -0.0136 S32:   0.0309 S33:   0.0183                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   403        E   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5470  13.8146 -15.7667              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0131 T22:   0.0374                                     
REMARK   3      T33:   0.0620 T12:   0.0195                                     
REMARK   3      T13:   0.0292 T23:   0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   404        E   404                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7320  10.2267 -16.8168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0618 T22:   0.0119                                     
REMARK   3      T33:   0.0145 T12:   0.0108                                     
REMARK   3      T13:   0.0275 T23:   0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0000                                     
REMARK   3      L33:   0.0000 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000                       
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000                       
REMARK   3      S31:   0.0000 S32:   0.0000 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4HPU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000075769.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66294                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.910                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLECULAR REPLACEMENT                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM BICINE, 150 MM AMMONIUM ACETATE,   
REMARK 280  10 MM DTT, ~7-10 MG/ML PROTEIN WELL SOLUTION: 2% MPD IN A 1 ML      
REMARK 280  WELL. 80 UL OF METHANOL WAS ADDED TO THE WELL IMMEDIATELY BEFORE    
REMARK 280  SEALING. DROP WAS 8 UL OF 1:1 PROTEIN:WELL, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 277.15K, PH 8.0                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.84500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.07000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.07000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.84500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.90000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY E     1                                                      
REMARK 465     ASN E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     ALA E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     ALA E     6                                                      
REMARK 465     LYS E     7                                                      
REMARK 465     LYS E     8                                                      
REMARK 465     GLY E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     GLU E    11                                                      
REMARK 465     ASP I    24                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN E  12    CG   CD   OE1  NE2                                  
REMARK 470     GLU E  13    CG   CD   OE1  OE2                                  
REMARK 470     SER E  14    OG                                                  
REMARK 470     PHE E 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS E 319    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU E   121     O    HOH E   598              1.99            
REMARK 500   OG   SER E   259     O    HOH E   641              2.02            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP E 166       45.50   -147.24                                   
REMARK 500    ASP E 184       78.80     63.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MYR E  401                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 404  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP I 600   O2G                                                    
REMARK 620 2 ANP I 600   O2A 152.5                                              
REMARK 620 3 ANP E 402   O2A 159.9   9.2                                        
REMARK 620 4 HOH E 596   O    94.8  88.1  91.9                                  
REMARK 620 5 ASN E 171   OD1 111.0  96.5  88.6  82.3                            
REMARK 620 6 ASP E 184   OD2  90.7  89.6  84.8 172.2  90.6                      
REMARK 620 7 ANP E 402   N3B  81.6  70.9  78.7  97.8 167.3  88.5                
REMARK 620 8 HOH I 747   O    24.5 153.3 152.4 115.3  99.2  68.9  92.3          
REMARK 620 9 ANP I 600   N3B  67.5  85.1  93.0  96.3 177.9  90.9  14.4  80.0    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH I 714   O                                                      
REMARK 620 2 SEP I  21   O1P 106.4                                              
REMARK 620 3 ANP I 600   O1B  99.1  94.3                                        
REMARK 620 4 ANP I 600   O3G 113.1   8.9  87.4                                  
REMARK 620 5 ANP E 402   O1B  93.1 100.0   7.3  93.6                            
REMARK 620 6 HOH E 595   O    91.6  86.5 168.6  92.1 170.5                      
REMARK 620 7 ASP E 184   OD2 158.3  94.8  83.9  88.5  87.9  84.7                
REMARK 620 8 ASP E 184   OD1 100.5 152.1  88.8 146.3  85.8  85.3  57.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP E 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP I 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT         
REMARK 800  PROTEIN KINASE INHIBITOR ALPHA                                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4HPT   RELATED DB: PDB                                   
REMARK 900 SAME COMPLEX DISPLAYING COMPLETE PHOSPHORYL TRANSFER                 
DBREF  4HPU E    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  4HPU I    5    24  UNP    P63248   IPKA_MOUSE       6     25             
SEQADV 4HPU ALA I   20  UNP  P63248    ASN    21 ENGINEERED MUTATION            
SEQADV 4HPU SEP I   21  UNP  P63248    ALA    22 ENGINEERED MUTATION            
SEQRES   1 E  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 E  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 E  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 E  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 E  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 E  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 E  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 E  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 E  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 E  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 E  350  HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA          
SEQRES  12 E  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 E  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 E  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 E  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 E  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 E  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 E  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 E  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 E  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 E  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 E  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 E  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 E  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 E  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 E  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 E  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 I   20  THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY          
SEQRES   2 I   20  ARG ARG ALA SEP ILE HIS ASP                                  
MODRES 4HPU SEP E  139  SER  PHOSPHOSERINE                                      
MODRES 4HPU TPO E  197  THR  PHOSPHOTHREONINE                                   
MODRES 4HPU SEP E  338  SER  PHOSPHOSERINE                                      
MODRES 4HPU SEP I   21  SER  PHOSPHOSERINE                                      
HET    SEP  E 139      10                                                       
HET    TPO  E 197      11                                                       
HET    SEP  E 338      10                                                       
HET    SEP  I  21      10                                                       
HET    MYR  E 401      10                                                       
HET    ANP  E 402      27                                                       
HET     MG  E 403       1                                                       
HET     MG  E 404       1                                                       
HET    ANP  I 600      31                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     MYR MYRISTIC ACID                                                    
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  SEP    3(C3 H8 N O6 P)                                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3  MYR    C14 H28 O2                                                   
FORMUL   4  ANP    2(C10 H17 N6 O12 P3)                                         
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   8  HOH   *432(H2 O)                                                    
HELIX    1   1 GLN E   12  THR E   32  1                                  21    
HELIX    2   2 GLN E   39  ASP E   41  5                                   3    
HELIX    3   3 LYS E   76  LEU E   82  1                                   7    
HELIX    4   4 GLN E   84  GLN E   96  1                                  13    
HELIX    5   5 GLU E  127  GLY E  136  1                                  10    
HELIX    6   6 SEP E  139  LEU E  160  1                                  22    
HELIX    7   7 LYS E  168  GLU E  170  5                                   3    
HELIX    8   8 THR E  201  LEU E  205  5                                   5    
HELIX    9   9 ALA E  206  LEU E  211  1                                   6    
HELIX   10  10 LYS E  217  GLY E  234  1                                  18    
HELIX   11  11 GLN E  242  GLY E  253  1                                  12    
HELIX   12  12 SER E  262  LEU E  273  1                                  12    
HELIX   13  13 VAL E  288  ASN E  293  1                                   6    
HELIX   14  14 HIS E  294  ALA E  298  5                                   5    
HELIX   15  15 ASP E  301  GLN E  307  1                                   7    
HELIX   16  16 THR I    6  ALA I   12  1                                   7    
SHEET    1   A 5 PHE E  43  THR E  51  0                                        
SHEET    2   A 5 GLY E  55  HIS E  62 -1  O  LEU E  59   N  LYS E  47           
SHEET    3   A 5 HIS E  68  ASP E  75 -1  O  MET E  71   N  MET E  58           
SHEET    4   A 5 ASN E 115  GLU E 121 -1  O  MET E 118   N  LYS E  72           
SHEET    5   A 5 LEU E 106  LYS E 111 -1  N  PHE E 108   O  VAL E 119           
SHEET    1   B 2 LEU E 162  ILE E 163  0                                        
SHEET    2   B 2 LYS E 189  ARG E 190 -1  O  LYS E 189   N  ILE E 163           
SHEET    1   C 2 LEU E 172  ILE E 174  0                                        
SHEET    2   C 2 ILE E 180  VAL E 182 -1  O  GLN E 181   N  LEU E 173           
LINK         C   PHE E 138                 N   SEP E 139     1555   1555  1.33  
LINK         C   SEP E 139                 N   GLU E 140     1555   1555  1.33  
LINK         C   TRP E 196                 N   TPO E 197     1555   1555  1.34  
LINK         C   TPO E 197                 N   LEU E 198     1555   1555  1.33  
LINK         C   VAL E 337                 N   SEP E 338     1555   1555  1.32  
LINK         C   SEP E 338                 N   ILE E 339     1555   1555  1.33  
LINK         C   ALA I  20                 N   SEP I  21     1555   1555  1.32  
LINK         C   SEP I  21                 N   ILE I  22     1555   1555  1.33  
LINK        MG    MG E 404                 O2GBANP I 600     1555   1555  1.77  
LINK        MG    MG E 403                 O   HOH I 714     1555   1555  1.83  
LINK         O1P SEP I  21                MG    MG E 403     1555   1555  1.96  
LINK        MG    MG E 403                 O1BBANP I 600     1555   1555  1.97  
LINK        MG    MG E 404                 O2ABANP I 600     1555   1555  2.02  
LINK        MG    MG E 403                 O3GBANP I 600     1555   1555  2.11  
LINK         O2AAANP E 402                MG    MG E 404     1555   1555  2.13  
LINK        MG    MG E 404                 O   HOH E 596     1555   1555  2.14  
LINK         O1BAANP E 402                MG    MG E 403     1555   1555  2.15  
LINK        MG    MG E 403                 O   HOH E 595     1555   1555  2.15  
LINK         OD1 ASN E 171                MG    MG E 404     1555   1555  2.20  
LINK         OD2 ASP E 184                MG    MG E 404     1555   1555  2.24  
LINK         OD2 ASP E 184                MG    MG E 403     1555   1555  2.26  
LINK         OD1 ASP E 184                MG    MG E 403     1555   1555  2.28  
LINK         N3BAANP E 402                MG    MG E 404     1555   1555  2.33  
LINK        MG    MG E 404                 O   HOH I 747     1555   1555  2.49  
LINK        MG    MG E 404                 N3BBANP I 600     1555   1555  2.55  
SITE     1 AC1  2 LEU E 152  GLU E 155                                          
SITE     1 AC2 23 VAL E  57  ALA E  70  LYS E  72  VAL E 104                    
SITE     2 AC2 23 MET E 120  GLU E 121  TYR E 122  VAL E 123                    
SITE     3 AC2 23 GLU E 127  GLU E 170  ASN E 171  LEU E 173                    
SITE     4 AC2 23 THR E 183  ASP E 184  PHE E 327   MG E 403                    
SITE     5 AC2 23  MG E 404  HOH E 521  HOH E 596  HOH E 740                    
SITE     6 AC2 23 ARG I  18  SEP I  21  HOH I 714                               
SITE     1 AC3  6 ASP E 184  ANP E 402  HOH E 595  SEP I  21                    
SITE     2 AC3  6 ANP I 600  HOH I 714                                          
SITE     1 AC4  6 ASN E 171  ASP E 184  ANP E 402  HOH E 596                    
SITE     2 AC4  6 ANP I 600  HOH I 747                                          
SITE     1 AC5 31 LEU E  49  GLY E  50  GLY E  52  VAL E  57                    
SITE     2 AC5 31 ALA E  70  LYS E  72  VAL E 104  MET E 120                    
SITE     3 AC5 31 GLU E 121  VAL E 123  GLU E 127  LYS E 168                    
SITE     4 AC5 31 GLU E 170  ASN E 171  LEU E 173  THR E 183                    
SITE     5 AC5 31 ASP E 184  PHE E 327   MG E 403   MG E 404                    
SITE     6 AC5 31 HOH E 521  HOH E 595  HOH E 596  ARG I  18                    
SITE     7 AC5 31 ALA I  20  SEP I  21  HOH I 702  HOH I 714                    
SITE     8 AC5 31 HOH I 729  HOH I 747  HOH I 750                               
SITE     1 AC6 77 THR E  51  SER E  53  LEU E  82  GLN E  84                    
SITE     2 AC6 77 GLU E  86  LEU E  89  ARG E  93  GLU E 127                    
SITE     3 AC6 77 PHE E 129  ARG E 133  LYS E 168  PRO E 169                    
SITE     4 AC6 77 GLU E 170  ASP E 184  PHE E 187  LYS E 189                    
SITE     5 AC6 77 ARG E 190  VAL E 191  LYS E 192  LEU E 198                    
SITE     6 AC6 77 CYS E 199  GLY E 200  THR E 201  GLU E 203                    
SITE     7 AC6 77 GLU E 230  TYR E 235  PRO E 236  PHE E 239                    
SITE     8 AC6 77 ALA E 240  ASP E 241  ILE E 246  TYR E 330                    
SITE     9 AC6 77 GLU E 349  ANP E 402   MG E 403  HOH E 514                    
SITE    10 AC6 77 HOH E 518  HOH E 592  HOH E 595  HOH E 728                    
SITE    11 AC6 77 HOH E 882  ANP I 600  HOH I 701  HOH I 703                    
SITE    12 AC6 77 HOH I 704  HOH I 705  HOH I 706  HOH I 707                    
SITE    13 AC6 77 HOH I 708  HOH I 709  HOH I 710  HOH I 711                    
SITE    14 AC6 77 HOH I 712  HOH I 713  HOH I 714  HOH I 715                    
SITE    15 AC6 77 HOH I 716  HOH I 717  HOH I 718  HOH I 719                    
SITE    16 AC6 77 HOH I 720  HOH I 721  HOH I 723  HOH I 726                    
SITE    17 AC6 77 HOH I 729  HOH I 731  HOH I 732  HOH I 735                    
SITE    18 AC6 77 HOH I 737  HOH I 740  HOH I 742  HOH I 744                    
SITE    19 AC6 77 HOH I 746  HOH I 747  HOH I 748  HOH I 749                    
SITE    20 AC6 77 HOH I 750                                                     
CRYST1   57.690   79.800   98.140  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017334  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012531  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010190        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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